Search Results

Overview

Uniprot IDQ6PJT7
Protein NameZinc finger CCCH domain-containing protein 14
Gene NameZC3H14
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
126 IPSARPEKRDSRVST
139 STSSQESKTTNVRQT
295 DENFRKRKLPVVSSV
307 SSVVKVKKFNHDGEE
348 RPSLPPSKQANKNLI
352 PPSKQANKNLILKAI
357 ANKNLILKAISEAQE
368 EAQESVTKTTNYSTV
378 NYSTVPQKQTLPVAP
470 DTRSFILKKPKLSEE
646 PNCKYDAKCTKPDCP
649 KYDAKCTKPDCPFTH
728 VPPRHALKWIRPQTS
99 DSNVPSNKSNFSRGD

Function

RNA-binding protein involved in the biogenesis of circular RNAs (circRNAs), which are produced by back-splicing circularization of pre-mRNAs (PubMed:39461343). Acts by binding to both exon-intron boundary and 3'-UTR of pre-mRNAs to promote circRNA biogenesis through dimerization and the association with the spliceosome (PubMed:39461343). Required for spermatogenesis via involvement in circRNA biogenesis (PubMed:39461343). Regulates the pre-mRNA processing of ATP5MC1; preventing its degradation (PubMed:27563065). Also binds the poly(A) tail of mRNAs; controlling poly(A) length in neuronal cells (PubMed:17630287, PubMed:24671764)

Protein Sequence

10 MEIGTEISRK 20 IRSAIKGKLQ 30 ELGAYVDEEL 40 PDYIMVMVAN 50 KKSQDQMTED 60 LSLFLGNNTI 70 RFTVWLHGVL 80 DKLRSVTTEP 90 SSLKSSDTNI 100 FDSNVPSNKS 110 NFSRGDERRH 120 EAAVPPLAIP 130 SARPEKRDSR 140 VSTSSQESKT 150 TNVRQTYDDG 160 AATRLMSTVK 170 PLREPAPSED 180 VIDIKPEPDD 190 LIDEDLNFVQ 200 ENPLSQKKPT 210 VTLTYGSSRP 220 SIEIYRPPAS 230 RNADSGVHLN 240 RLQFQQQQNS 250 IHAAKQLDMQ 260 SSWVYETGRL 270 CEPEVLNSLE 280 ETYSPFFRNN 290 SEKMSMEDEN 300 FRKRKLPVVS 310 SVVKVKKFNH 320 DGEEEEEDDD 330 YGSRTGSISS 340 SVSVPAKPER 350 RPSLPPSKQA 360 NKNLILKAIS 370 EAQESVTKTT 380 NYSTVPQKQT 390 LPVAPRTRTS 400 QEELLAEVVQ 410 GQSRTPRISP 420 PIKEEETKGD 430 SVEKNQGTQQ 440 RQLLSRLQID 450 PVMAETLQMS 460 QDYYDMESMV 470 HADTRSFILK 480 KPKLSEEVVV 490 APNQESGMKT 500 ADSLRVLSGH 510 LMQTRDLVQP 520 DKPASPKFIV 530 TLDGVPSPPG 540 YMSDQEEDMC 550 FEGMKPVNQT 560 AASNKGLRGL 570 LHPQQLHLLS 580 RQLEDPNGSF 590 SNAEMSELSV 600 AQKPEKLLER 610 CKYWPACKNG 620 DECAYHHPIS 630 PCKAFPNCKF 640 AEKCLFVHPN 650 CKYDAKCTKP 660 DCPFTHVSRR 670 IPVLSPKPAV 680 APPAPPSSSQ 690 LCRYFPACKK 700 MECPFYHPKH 710 CRFNTQCTRP 720 DCTFYHPTIN 730 VPPRHALKWI RPQTSE

Gene Ontology

Classification GO ID Description
Cellular Component GO:1904115 axon cytoplasm
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0032839 dendrite cytoplasm
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0008143 poly(A) binding
Molecular Function GO:0036002 pre-mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0030154 cell differentiation
Biological Process GO:0048255 mRNA stabilization
Biological Process GO:0043488 regulation of mRNA stability
Biological Process GO:0007283 spermatogenesis
Biological Process GO:0160091 spliceosome-depend formation of circular RNA

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.